ArticleFrontiers in cellular neuroscience2013
Dynamic micro-organization of P2X7 receptors revealed by PALM based single particle tracking.
Article in Frontiers in cellular neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Affinity-guided labeling reveals P2X7 nanoscale membrane redistribution during BV2 microglial activation.eLife · 2026Article
- P2X7 Receptors and TMEM16 Channels Are Functionally Coupled with Implications for Macropore Formation and Current Facilitation.International journal of molecular sciences · 2021Article
- Molecular Crowding and Diffusion-Capture in Synapses.iScience · 2020Article
- Clustering of Tau fibrils impairs the synaptic composition of α3-NaThe EMBO journal · 2019Article
- P2X receptor overexpression induced by soluble oligomers of amyloid beta peptide potentiates synaptic failure and neuronal dyshomeostasis in cellular models of Alzheimer's disease.Neuropharmacology · 2018Article
- Cannabinoid Receptors Modulate Neuronal Morphology and AnkyrinG Density at the Axon Initial Segment.Frontiers in cellular neuroscience · 2017Article
- The Nanoworld of the Tripartite Synapse: Insights from Super-Resolution Microscopy.Frontiers in cellular neuroscience · 2017Article
- P2X7R large pore is partially blocked by pore forming proteins antagonists in astrocytes.Journal of bioenergetics and biomembranes · 2016Article
- Applying superresolution localization-based microscopy to neurons.Synapse (New York, N.Y.) · 2015Review
- Tracking the activity-dependent diffusion of synaptic proteins using restricted photoconversion of Dendra2.Frontiers in cellular neuroscience · 2015Article
- Imaging P2X4 receptor subcellular distribution, trafficking, and regulation using P2X4-pHluorin.The Journal of general physiology · 2014Article
- ATP-gated P2X receptors in health and disease.Frontiers in cellular neuroscience · 2014Article
- Cell-surface translational dynamics of nicotinic acetylcholine receptors.Frontiers in synaptic neuroscience · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenosine triphosphate (ATP)-gated P2X7 receptors (P2X7Rs) are members of the purinergic receptor family that are expressed in several cell types including neurons. A high concentration of ATP is required for the channel opening of P2X7Rs compared to other members of this receptor family. Recent work suggests that ATP binding to members of the P2X receptor family determines the diffusion and localization of these receptors on the plasma membrane of neurons. Here, we employed single particle tracking photoactivated localization microscopy (sptPALM) to study the diffusion and ATP-dependence of rat P2X7Rs. Dendra2-tagged P2X7Rs were transfected in hippocampal neurons and imaged on proximal dendrites. Our results suggest the presence of two populations of P2X7Rs within the extra-synaptic membrane: a population composed of rapidly diffusing receptors and one stabilized within nanoclusters (~100 nm diameter). P2X7R trajectories were rarely observed at synaptic sites. P2X7R mutations in the ATP-binding site (K64A) or the conserved phosphorylation site (K17A) resulted in faster- and slower-diffusing receptors, respectively. Furthermore, ATP differentially accelerated wild type and K17A-mutant receptors but not K64A-mutant receptors. Our results indicate that receptor conformation plays a critical role in regulating ATP-mediated changes in P2X7R diffusion and micro-organization.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.